GenomeNet

Database: PDB
Entry: 5YLW
LinkDB: 5YLW
Original site: 5YLW 
HEADER    OXIDOREDUCTASE                          20-OCT-17   5YLW              
TITLE     CYP76AH1 FROM SALVIA MILTIORRHIZA                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FERRUGINOL SYNTHASE;                                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CYTOCHROME P450 76AH1;                                      
COMPND   5 EC: 1.14.13.190;                                                     
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SALVIA MILTIORRHIZA;                            
SOURCE   3 ORGANISM_COMMON: CHINESE SAGE;                                       
SOURCE   4 ORGANISM_TAXID: 226208;                                              
SOURCE   5 GENE: CYP76AH1;                                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI-THERMUS THERMOPHILUS SHUTTLE     
SOURCE   7 VECTOR PTRH1T;                                                       
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 1085940                                     
KEYWDS    P450, MONOXYGENASE, BIOSYNTHETIC PROTEIN, OXIDOREDUCTASE              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.CHANG                                                               
REVDAT   1   24-OCT-18 5YLW    0                                                
JRNL        AUTH   Z.CHANG                                                      
JRNL        TITL   CYP76AH1 FROM SALVIA MILTIORRHIZA                            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.39                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 75533                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.139                           
REMARK   3   R VALUE            (WORKING SET) : 0.137                           
REMARK   3   FREE R VALUE                     : 0.168                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4021                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.74                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5219                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.99                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2200                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 264                          
REMARK   3   BIN FREE R VALUE                    : 0.2500                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3667                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 44                                      
REMARK   3   SOLVENT ATOMS            : 610                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.12000                                             
REMARK   3    B22 (A**2) : -0.12000                                             
REMARK   3    B33 (A**2) : 0.19000                                              
REMARK   3    B12 (A**2) : -0.06000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.086         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.071         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.039         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.565         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.970                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4040 ; 0.010 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5530 ; 1.915 ; 1.989       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   538 ; 5.232 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   176 ;34.144 ;23.580       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   741 ;12.138 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;18.780 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   607 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3083 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  4040 ; 2.048 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):    53 ;33.380 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  4468 ;12.795 ; 5.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 5YLW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-OCT-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300005319.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-DEC-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NFPSS                              
REMARK 200  BEAMLINE                       : BL19U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97853                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 79803                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 24.1500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: MORDA                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.22                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, JEFFAMINE M-600 REAGENT,          
REMARK 280  MANGANESE CHLORIDE, VAPOR DIFFUSION, TEMPERATURE 289K               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       35.33000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       70.66000            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       70.66000            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       35.33000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     PHE A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     LEU A    10                                                      
REMARK 465     PHE A    11                                                      
REMARK 465     PHE A    12                                                      
REMARK 465     ILE A    13                                                      
REMARK 465     ALA A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     THR A    16                                                      
REMARK 465     ILE A    17                                                      
REMARK 465     THR A    18                                                      
REMARK 465     PHE A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     SER A    21                                                      
REMARK 465     PHE A    22                                                      
REMARK 465     ARG A    23                                                      
REMARK 465     ARG A    24                                                      
REMARK 465     ARG A    25                                                      
REMARK 465     ARG A    26                                                      
REMARK 465     ASN A    27                                                      
REMARK 465     LYS A   494                                                      
REMARK 465     SER A   495                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER A   161     NH1  ARG A   163              2.01            
REMARK 500   O    HOH A   885     O    HOH A   974              2.16            
REMARK 500   O    HOH A   797     O    HOH A  1062              2.16            
REMARK 500   O    HOH A   607     O    HOH A  1104              2.17            
REMARK 500   O    ASN A   416     O    HOH A   601              2.18            
REMARK 500   O    HOH A  1078     O    HOH A  1085              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  1070     O    HOH A  1128     3654     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ILE A  37      -65.73     72.24                                   
REMARK 500    HIS A  86      -64.35   -109.46                                   
REMARK 500    ALA A 117     -167.65   -160.34                                   
REMARK 500    ASP A 192       58.65   -102.99                                   
REMARK 500    SER A 300      -74.18    -87.29                                   
REMARK 500    LEU A 366     -142.46     48.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1209        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH A1210        DISTANCE =  6.65 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A 502  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 102   ND1                                                    
REMARK 620 2 HOH A 646   O    94.2                                              
REMARK 620 3 HOH A 780   O    84.7  75.6                                        
REMARK 620 4 HOH A 979   O    83.2 166.2  90.6                                  
REMARK 620 5 HOH A 937   O   108.1 102.4 167.3  91.3                            
REMARK 620 6 HOH A 902   O   167.8  90.6  85.7  89.5  81.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 501  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 437   SG                                                     
REMARK 620 2 HEM A 501   NA  102.9                                              
REMARK 620 3 HEM A 501   NB   92.7  88.9                                        
REMARK 620 4 HEM A 501   NC   93.1 164.0  89.6                                  
REMARK 620 5 HEM A 501   ND   98.6  87.2 168.5  91.2                            
REMARK 620 6 HOH A 771   O   172.2  84.9  86.4  79.1  82.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MN A 502                  
DBREF  5YLW A    1   495  UNP    S4UX02   CYPH1_SALMI      1    495             
SEQRES   1 A  495  MET ASP SER PHE PRO LEU LEU ALA ALA LEU PHE PHE ILE          
SEQRES   2 A  495  ALA ALA THR ILE THR PHE LEU SER PHE ARG ARG ARG ARG          
SEQRES   3 A  495  ASN LEU PRO PRO GLY PRO PHE PRO TYR PRO ILE VAL GLY          
SEQRES   4 A  495  ASN MET LEU GLN LEU GLY ALA ASN PRO HIS GLN VAL PHE          
SEQRES   5 A  495  ALA LYS LEU SER LYS ARG TYR GLY PRO LEU MET SER ILE          
SEQRES   6 A  495  HIS LEU GLY SER LEU TYR THR VAL ILE VAL SER SER PRO          
SEQRES   7 A  495  GLU MET ALA LYS GLU ILE LEU HIS ARG HIS GLY GLN VAL          
SEQRES   8 A  495  PHE SER GLY ARG THR ILE ALA GLN ALA VAL HIS ALA CYS          
SEQRES   9 A  495  ASP HIS ASP LYS ILE SER MET GLY PHE LEU PRO VAL ALA          
SEQRES  10 A  495  SER GLU TRP ARG ASP MET ARG LYS ILE CYS LYS GLU GLN          
SEQRES  11 A  495  MET PHE SER ASN GLN SER MET GLU ALA SER GLN GLY LEU          
SEQRES  12 A  495  ARG ARG GLN LYS LEU GLN GLN LEU LEU ASP HIS VAL GLN          
SEQRES  13 A  495  LYS CYS SER ASP SER GLY ARG ALA VAL ASP ILE ARG GLU          
SEQRES  14 A  495  ALA ALA PHE ILE THR THR LEU ASN LEU MET SER ALA THR          
SEQRES  15 A  495  LEU PHE SER SER GLN ALA THR GLU PHE ASP SER LYS ALA          
SEQRES  16 A  495  THR MET GLU PHE LYS GLU ILE ILE GLU GLY VAL ALA THR          
SEQRES  17 A  495  ILE VAL GLY VAL PRO ASN PHE ALA ASP TYR PHE PRO ILE          
SEQRES  18 A  495  LEU ARG PRO PHE ASP PRO GLN GLY VAL LYS ARG ARG ALA          
SEQRES  19 A  495  ASP VAL PHE PHE GLY LYS LEU LEU ALA LYS ILE GLU GLY          
SEQRES  20 A  495  TYR LEU ASN GLU ARG LEU GLU SER LYS ARG ALA ASN PRO          
SEQRES  21 A  495  ASN ALA PRO LYS LYS ASP ASP PHE LEU GLU ILE VAL VAL          
SEQRES  22 A  495  ASP ILE ILE GLN ALA ASN GLU PHE LYS LEU LYS THR HIS          
SEQRES  23 A  495  HIS PHE THR HIS LEU MET LEU ASP LEU PHE VAL GLY GLY          
SEQRES  24 A  495  SER ASP THR ASN THR THR SER ILE GLU TRP ALA MET SER          
SEQRES  25 A  495  GLU LEU VAL MET ASN PRO ASP LYS MET ALA ARG LEU LYS          
SEQRES  26 A  495  ALA GLU LEU LYS SER VAL ALA GLY ASP GLU LYS ILE VAL          
SEQRES  27 A  495  ASP GLU SER ALA MET PRO LYS LEU PRO TYR LEU GLN ALA          
SEQRES  28 A  495  VAL ILE LYS GLU VAL MET ARG ILE HIS PRO PRO GLY PRO          
SEQRES  29 A  495  LEU LEU LEU PRO ARG LYS ALA GLU SER ASP GLN GLU VAL          
SEQRES  30 A  495  ASN GLY TYR LEU ILE PRO LYS GLY THR GLN ILE LEU ILE          
SEQRES  31 A  495  ASN ALA TYR ALA ILE GLY ARG ASP PRO SER ILE TRP THR          
SEQRES  32 A  495  ASP PRO GLU THR PHE ASP PRO GLU ARG PHE LEU ASP ASN          
SEQRES  33 A  495  LYS ILE ASP PHE LYS GLY GLN ASP TYR GLU LEU LEU PRO          
SEQRES  34 A  495  PHE GLY SER GLY ARG ARG VAL CYS PRO GLY MET PRO LEU          
SEQRES  35 A  495  ALA THR ARG ILE LEU HIS MET ALA THR ALA THR LEU VAL          
SEQRES  36 A  495  HIS ASN PHE ASP TRP LYS LEU GLU ASP ASP SER THR ALA          
SEQRES  37 A  495  ALA ALA ASP HIS ALA GLY GLU LEU PHE GLY VAL ALA VAL          
SEQRES  38 A  495  ARG ARG ALA VAL PRO LEU ARG ILE ILE PRO ILE VAL LYS          
SEQRES  39 A  495  SER                                                          
HET    HEM  A 501      43                                                       
HET     MN  A 502       1                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM      MN MANGANESE (II) ION                                               
HETSYN     HEM HEME                                                             
FORMUL   2  HEM    C34 H32 FE N4 O4                                             
FORMUL   3   MN    MN 2+                                                        
FORMUL   4  HOH   *610(H2 O)                                                    
HELIX    1 AA1 ASN A   40  LEU A   44  5                                   5    
HELIX    2 AA2 ASN A   47  GLY A   60  1                                  14    
HELIX    3 AA3 SER A   77  HIS A   86  1                                  10    
HELIX    4 AA4 ALA A   98  ILE A  109  5                                  12    
HELIX    5 AA5 ALA A  117  GLN A  130  1                                  14    
HELIX    6 AA6 SER A  133  SER A  140  1                                   8    
HELIX    7 AA7 SER A  140  GLY A  162  1                                  23    
HELIX    8 AA8 ILE A  167  SER A  185  1                                  19    
HELIX    9 AA9 SER A  193  GLY A  211  1                                  19    
HELIX   10 AB1 ASN A  214  PHE A  219  1                                   6    
HELIX   11 AB2 PRO A  220  ASP A  226  5                                   7    
HELIX   12 AB3 GLY A  229  ASN A  259  1                                  31    
HELIX   13 AB4 ASP A  267  ASN A  279  1                                  13    
HELIX   14 AB5 LYS A  284  GLY A  299  1                                  16    
HELIX   15 AB6 GLY A  299  ASN A  317  1                                  19    
HELIX   16 AB7 ASN A  317  GLY A  333  1                                  17    
HELIX   17 AB8 ASP A  339  LYS A  345  5                                   7    
HELIX   18 AB9 LEU A  346  HIS A  360  1                                  15    
HELIX   19 AC1 ASN A  391  ARG A  397  1                                   7    
HELIX   20 AC2 ASP A  409  LEU A  414  5                                   6    
HELIX   21 AC3 SER A  432  VAL A  436  5                                   5    
HELIX   22 AC4 GLY A  439  PHE A  458  1                                  20    
HELIX   23 AC5 THR A  467  GLY A  474  1                                   8    
SHEET    1 AA1 4 LEU A  62  LEU A  67  0                                        
SHEET    2 AA1 4 LEU A  70  VAL A  75 -1  O  ILE A  74   N  MET A  63           
SHEET    3 AA1 4 GLN A 387  ILE A 390  1  O  LEU A 389   N  VAL A  75           
SHEET    4 AA1 4 ARG A 369  LYS A 370 -1  N  ARG A 369   O  ILE A 388           
SHEET    1 AA2 3 VAL A 165  ASP A 166  0                                        
SHEET    2 AA2 3 ARG A 488  ILE A 492 -1  O  ILE A 489   N  VAL A 165           
SHEET    3 AA2 3 ASP A 459  LEU A 462 -1  N  LYS A 461   O  ILE A 490           
SHEET    1 AA3 2 GLN A 375  VAL A 377  0                                        
SHEET    2 AA3 2 TYR A 380  ILE A 382 -1  O  TYR A 380   N  VAL A 377           
SHEET    1 AA4 2 GLU A 475  LEU A 476  0                                        
SHEET    2 AA4 2 ARG A 482  ARG A 483 -1  O  ARG A 482   N  LEU A 476           
LINK         ND1 HIS A 102                MN    MN A 502     1555   1555  2.26  
LINK         SG  CYS A 437                FE   HEM A 501     1555   1555  2.34  
LINK        FE   HEM A 501                 O   HOH A 771     1555   1555  2.36  
LINK        MN    MN A 502                 O   HOH A 646     1555   1555  2.40  
LINK        MN    MN A 502                 O   HOH A 780     1555   1555  1.85  
LINK        MN    MN A 502                 O   HOH A 979     1555   1555  2.26  
LINK        MN    MN A 502                 O   HOH A 937     1555   1555  2.09  
LINK        MN    MN A 502                 O   HOH A 902     1555   4655  2.14  
SITE     1 AC1 23 ARG A  95  MET A 111  GLY A 112  TRP A 120                    
SITE     2 AC1 23 ARG A 124  PHE A 132  LEU A 295  GLY A 298                    
SITE     3 AC1 23 GLY A 299  THR A 302  ASN A 303  PRO A 362                    
SITE     4 AC1 23 LEU A 366  ARG A 369  PRO A 429  PHE A 430                    
SITE     5 AC1 23 GLY A 431  SER A 432  ARG A 435  CYS A 437                    
SITE     6 AC1 23 PRO A 438  GLY A 439  HOH A 771                               
SITE     1 AC2  6 HIS A 102  HOH A 646  HOH A 780  HOH A 902                    
SITE     2 AC2  6 HOH A 937  HOH A 979                                          
CRYST1  108.776  108.776  105.990  90.00  90.00 120.00 P 31 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009193  0.005308  0.000000        0.00000                         
SCALE2      0.000000  0.010615  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009435        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system